메뉴 건너뛰기




Volumn 18, Issue 17, 2013, Pages 2274-2283

Hemoglobin redox reactions and red blood cell aging

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; HEMOGLOBIN; NITRIC OXIDE; NITRITE; PEROXYNITRITE; POTASSIUM;

EID: 84876892476     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4867     Document Type: Review
Times cited : (124)

References (104)
  • 1
    • 0018177245 scopus 로고
    • Influence of mouse age and erythrocyte age on glutathione metabolism
    • Abraham EC, Taylor JF, and Lang CA. Influence of mouse age and erythrocyte age on glutathione metabolism. Biochem J 174: 819-825, 1978. (Pubitemid 9015255)
    • (1978) Biochemical Journal , vol.174 , Issue.3 , pp. 819-825
    • Abraham, E.C.1    Fuller Taylor, J.2    Lang, C.A.3
  • 2
    • 0028061399 scopus 로고
    • Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium
    • Abugo OO and Rifkind JM. Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium. J Biol Chem 269: 24845-24853, 1994. (Pubitemid 24311745)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.40 , pp. 24845-24853
    • Abugo, O.O.1    Rifkind, J.M.2
  • 4
    • 0031906904 scopus 로고    scopus 로고
    • Hemorheological changes during human aging
    • DOI 10.1159/000021993
    • Ajmani RS and Rifkind JM. Hemorheological changes during human aging. Gerontology 44: 111-120, 1998. (Pubitemid 28075141)
    • (1998) Gerontology , vol.44 , Issue.2 , pp. 111-120
    • Ajmani, R.S.1    Rifkind, J.M.2
  • 5
    • 78049383203 scopus 로고    scopus 로고
    • Aging and death signalling in mature red cells: From basic science to transfusion practice
    • Antonelou MH, Kriebardis AG, and Papassideri IS. Aging and death signalling in mature red cells: from basic science to transfusion practice. Blood Transfus 8 Suppl 3: s39-s47, 2010.
    • (2010) Blood Transfus 8 Suppl , vol.3
    • Antonelou, M.H.1    Kriebardis, A.G.2    Papassideri, I.S.3
  • 6
    • 0033151515 scopus 로고    scopus 로고
    • Red blood cells inhibit apoptosis of human neutrophils
    • Aoshiba K, Nakajima Y, Yasui S, Tamaoki J, and Nagai A. Red blood cells inhibit apoptosis of human neutrophils. Blood 93: 4006-4010, 1999. (Pubitemid 29249850)
    • (1999) Blood , vol.93 , Issue.11 , pp. 4006-4010
    • Aoshiba, K.1    Nakajima, Y.2    Yasui, S.3    Tamaoki, J.4    Nagai, A.5
  • 7
    • 0029930628 scopus 로고    scopus 로고
    • Production of superoxide from hemoglobin-bound oxygen under hypoxic conditions
    • DOI 10.1021/bi952875+
    • Balagopalakrishna C, Manoharan PT, Abugo OO, and Rifkind JM. Production of superoxide from hemoglobinbound oxygen under hypoxic conditions. Biochemistry 35: 6393-6398, 1996. (Pubitemid 26164073)
    • (1996) Biochemistry , vol.35 , Issue.20 , pp. 6393-6398
    • Balagopalakrishna, C.1    Manoharan, P.T.2    Abugo, O.O.3    Rifkind, J.M.4
  • 8
    • 0026036015 scopus 로고
    • Erythrocyte aging: Physical and chemical membrane changes
    • Bartosz G. Erythrocyte aging: physical and chemical membrane changes. Gerontology 37: 33-67, 1991.
    • (1991) Gerontology , vol.37 , pp. 33-67
    • Bartosz, G.1
  • 9
    • 0020402181 scopus 로고
    • Aging of the erythrocyte. XIV. ATP content does decrease
    • Bartosz G, Grzelinska E, and Wagner J. Aging of the erythrocyte. XIV. ATP content does decrease. Experientia 38: 575, 1982.
    • (1982) Experientia , vol.38 , pp. 575
    • Bartosz, G.1    Grzelinska, E.2    Wagner, J.3
  • 10
    • 0020355588 scopus 로고
    • Aging of the erythrocyte. XVII. Binding of autologous immunoglobulin G
    • DOI 10.1016/0047-6374(82)90089-6
    • Bartosz G, Soszynski M, and Wasilewski A. Aging of the erythrocyte. XVII. Binding of autologous immunoglobulin G. Mech Ageing Dev 20: 223-232, 1982. (Pubitemid 13155469)
    • (1982) Mechanisms of Ageing and Development , vol.20 , Issue.3 , pp. 223-232
    • Bartosz, G.1    Soszynski, M.2    Wasilewski, A.3
  • 11
    • 12444257346 scopus 로고    scopus 로고
    • Erythrocyte signal transduction pathways, their oxygenation dependence and functional significance
    • Barvitenko NN, Adragna NC, and Weber RE. Erythrocyte signal transduction pathways, their oxygenation dependence and functional significance. Cell Physiol Biochem 15: 1-18, 2005.
    • (2005) Cell Physiol Biochem , vol.15 , pp. 1-18
    • Barvitenko, N.N.1    Adragna, N.C.2    Weber, R.E.3
  • 12
    • 37549067544 scopus 로고    scopus 로고
    • Hemoglobin depletion from red blood cell cytosol reveals new proteins in 2-D gel-based proteomics study
    • Bhattacharya D, Mukhopadhyay D, and Chakrabarti A. Hemoglobin depletion from red blood cell cytosol reveals new proteins in 2-D gel-based proteomics study. Proteomics Clin Appl 1: 561-564, 2007.
    • (2007) Proteomics Clin Appl , vol.1 , pp. 561-564
    • Bhattacharya, D.1    Mukhopadhyay, D.2    Chakrabarti, A.3
  • 13
    • 0027475338 scopus 로고
    • Membrane transport of Na and K and cell dehydration in sickle erythrocytes
    • Brugnara C. Membrane transport of Na, and K and cell dehydration in sickle erythrocytes. Experientia 49: 100-109, 1993. (Pubitemid 23063409)
    • (1993) Experientia , vol.49 , Issue.2 , pp. 100-109
    • Brugnara, C.1
  • 14
    • 70349610358 scopus 로고    scopus 로고
    • Nitrite enhances RBC hypoxic ATP synthesis and the release of ATP into the vasculature: A new mechanism for nitrite-induced vasodilation
    • Cao Z, Bell JB, Mohanty JG, Nagababu E, and Rifkind JM. Nitrite enhances RBC hypoxic ATP synthesis and the release of ATP into the vasculature: a new mechanism for nitrite-induced vasodilation. Am J Physiol Heart Circ Physiol 297: H1494-H1503, 2009.
    • (2009) Am J Physiol Heart Circ Physiol , vol.297
    • Cao, Z.1    Bell, J.B.2    Mohanty, J.G.3    Nagababu, E.4    Rifkind, J.M.5
  • 15
    • 33947140920 scopus 로고    scopus 로고
    • Peroxynitrite oxidizes erythrocyte membrane band 3 protein and diminishes its anion transport capacity
    • DOI 10.1080/10715760601090305, PII 773175658
    • Celedon G, Gonzalez G, Pino J, and Lissi EA. Peroxynitrite oxidizes erythrocyte membrane band 3 protein and diminishes its anion transport capacity. Free Radic Res 41: 316-323, 2007. (Pubitemid 46404474)
    • (2007) Free Radical Research , vol.41 , Issue.3 , pp. 316-323
    • Celedo, G.1    Gonzalez, G.2    Pino, J.3    Lissi, E.4
  • 16
    • 38349184814 scopus 로고    scopus 로고
    • Characterization of the deoxyhemoglobin binding site on human erythrocyte band 3: Implications for O2 regulation of erythrocyte properties
    • Chu H, Breite A, Ciraolo P, Franco RS, and Low PS. Characterization of the deoxyhemoglobin binding site on human erythrocyte band 3: implications for O2 regulation of erythrocyte properties. Blood 111: 932-938, 2008.
    • (2008) Blood , vol.111 , pp. 932-938
    • Chu, H.1    Breite, A.2    Ciraolo, P.3    Franco, R.S.4    Low, P.S.5
  • 17
    • 39649106568 scopus 로고    scopus 로고
    • Free radical metabolism in human erythrocytes
    • Cimen MY. Free radical metabolism in human erythrocytes. Clin Chim Acta 390: 1-11, 2008.
    • (2008) Clin Chim Acta , vol.390 , pp. 1-11
    • Cimen, M.Y.1
  • 18
    • 0036532552 scopus 로고    scopus 로고
    • Iron release, oxidative stress and erythrocyte ageing
    • DOI 10.1016/S0891-5849(02)00759-1, PII S0891584902007591
    • Comporti M, Signorini C, Buonocore G, and Ciccoli L. Iron release, oxidative stress and erythrocyte ageing. Free Radic Biol Med 32: 568-576, 2002. (Pubitemid 34241489)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.7 , pp. 568-576
    • Comporti, M.1    Signorini, C.2    Buonocore, G.3    Ciccoli, L.4
  • 19
    • 0032951905 scopus 로고    scopus 로고
    • Nitric oxide and iron proteins
    • DOI 10.1016/S0005-2728(99)00021-3, PII S0005272899000213
    • Cooper CE. Nitric oxide and iron proteins. Biochim Biophys Acta 1411: 290-309, 1999. (Pubitemid 29221956)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1411 , Issue.2-3 , pp. 290-309
    • Cooper, C.E.1
  • 21
    • 0025251722 scopus 로고
    • Density fractionation of erythrocytes by Percoll/hypaque results in only a slight enrichment for aged cells
    • Dale GL and Norenberg SL. Density fractionation of erythrocytes by Percoll/hypaque results in only a slight enrichment for aged cells. Biochim Biophys Acta 1036: 183-187, 1990.
    • (1990) Biochim Biophys Acta , vol.1036 , pp. 183-187
    • Dale, G.L.1    Norenberg, S.L.2
  • 22
    • 41949133917 scopus 로고    scopus 로고
    • Regulation of phospholipid asymmetry in the erythrocyte membrane
    • DOI 10.1097/MOH.0b013e3282f97af7, PII 0006275220080500000007
    • Daleke DL. Regulation of phospholipid asymmetry in the erythrocyte membrane. Curr Opin Hematol 15: 191-195, 2008. (Pubitemid 351507569)
    • (2008) Current Opinion in Hematology , vol.15 , Issue.3 , pp. 191-195
    • Daleke, D.L.1
  • 24
    • 0037047013 scopus 로고    scopus 로고
    • Binding of hemoglobin to red cell membranes with eosin-5-maleimide- labeled band 3: Analysis of centrifugation and fluorescence lifetime data
    • DOI 10.1021/bi012007e
    • Demehin AA, Abugo OO, Jayakumar R, Lakowicz JR, and Rifkind JM. Binding of hemoglobin to red cell membranes with eosin-5-maleimide-labeled band 3: analysis of centrifugation and fluorescence data. Biochemistry 41: 8630-8637, 2002. (Pubitemid 34743302)
    • (2002) Biochemistry , vol.41 , Issue.27 , pp. 8630-8637
    • Demehin, A.A.1    Abugo, O.O.2    Jayakumar, R.3    Lakowicz, J.R.4    Rifkind, J.M.5
  • 26
    • 0019807744 scopus 로고
    • Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites
    • Doyle MP, Pickering RA, DeWeert TM, Hoekstra JW, and Pater D. Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites. J Biol Chem 256: 12393-12398, 1981. (Pubitemid 12141507)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.23 , pp. 12393-12398
    • Doyle, M.P.1    Pickering, R.A.2    DeWeert, T.M.3
  • 27
    • 0023652842 scopus 로고
    • Effect of shape, membrane deformability and phospholipid organization on phosphate-calcium-induced fusion of erythrocytes
    • Farooqui SM, Wali RK, Baker RF, and Kalra VK. Effect of cell shape, membrane deformability and phospholipid organization on phosphate-calcium- induced fusion of erythrocytes. Biochim Biophys Acta 904: 239-250, 1987. (Pubitemid 17158400)
    • (1987) Biochimica et Biophysica Acta - Biomembranes , vol.904 , Issue.2 , pp. 239-250
    • Farooqui, S.M.1    Wali, R.K.2    Baker, R.F.3    Kalra, V.K.4
  • 29
    • 55049140968 scopus 로고    scopus 로고
    • Erythrocyte programmed cell death
    • Foller M, Huber SM, and Lang F. Erythrocyte programmed cell death. IUBMB Life 60: 661-668, 2008.
    • (2008) IUBMB Life , vol.60 , pp. 661-668
    • Foller, M.1    Huber, S.M.2    Lang, F.3
  • 31
    • 33645780634 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase in vascular disease: From marvel to menace
    • Forstermann U and Munzel T. Endothelial nitric oxide synthase in vascular disease: from marvel to menace. Circulation 113: 1708-1714, 2006.
    • (2006) Circulation , vol.113 , pp. 1708-1714
    • Forstermann, U.1    Munzel, T.2
  • 32
    • 0028237681 scopus 로고
    • Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells
    • Giulivi C and Davies KJ. Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells. Methods Enzymol 231: 490-496, 1994.
    • (1994) Methods Enzymol , vol.231 , pp. 490-496
    • Giulivi, C.1    Davies, K.J.2
  • 33
    • 0021330550 scopus 로고
    • Decreased enzymic protection and increased sensitivity to oxidative damage in erythrocytes as a function of cell and donor aging
    • Glass GA and Gershon D. Decreased enzymic protection and increased sensitivity to oxidative damage in erythrocytes as a function of cell and donor aging. Biochem J 218: 531-537, 1984.
    • (1984) Biochem J , vol.218 , pp. 531-537
    • Glass, G.A.1    Gershon, D.2
  • 34
    • 55549095980 scopus 로고    scopus 로고
    • The increase in plasma nitrite after a dietary nitrate load is markedly attenuated by an antibacterial mouthwash
    • Govoni M, Jansson EA, Weitzberg E, and Lundberg JO. The increase in plasma nitrite after a dietary nitrate load is markedly attenuated by an antibacterial mouthwash. Nitric Oxide 19: 333-337, 2008.
    • (2008) Nitric Oxide , vol.19 , pp. 333-337
    • Govoni, M.1    Jansson, E.A.2    Weitzberg, E.3    Lundberg, J.O.4
  • 38
    • 0022512734 scopus 로고
    • Glutathione-linked enzyme activities in red cell aging
    • DOI 10.1016/0009-8981(86)90168-3
    • Imanishi H, Nakai T, Abe T, and Takino T. Glutathionelinked enzyme activities in red cell aging. Clin Chim Acta 159: 73-76, 1986. (Pubitemid 16026299)
    • (1986) Clinica Chimica Acta , vol.159 , Issue.1 , pp. 73-76
    • Imanishi, H.1    Nakai, T.2    Abe, T.3    Takino, T.4
  • 39
    • 0023814970 scopus 로고
    • Isolation and characterization of the hemichrome-stabilized membrane protein aggregates from sickle erythrocytes. Major site of autologous antibody binding
    • Kannan R, Labotka R, and Low PS. Isolation and characterization of the hemichrome-stabilized membrane protein aggregates from sickle erythrocytes. Major site of autologous antibody binding. J Biol Chem 263: 13766-13773, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 13766-13773
    • Kannan, R.1    Labotka, R.2    Low, P.S.3
  • 40
    • 0027566866 scopus 로고
    • Generation of senescent cell antigen on old cells initiates IgG binding to a neoantigen
    • Kay MM. Generation of senescent cell antigen on old cells initiates IgG binding to a neoantigen. Cell Mol Biol (Noisyle-grand) 39: 131-153, 1993.
    • (1993) Cell Mol Biol (Noisyle-grand) , vol.39 , pp. 131-153
    • Kay, M.M.1
  • 41
    • 44349096391 scopus 로고    scopus 로고
    • The reaction between nitrite and oxyhemoglobin: A mechanistic study
    • Keszler A, Piknova B, Schechter AN, and Hogg N. The reaction between nitrite and oxyhemoglobin: a mechanistic study. J Biol Chem 283: 9615-9622, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 9615-9622
    • Keszler, A.1    Piknova, B.2    Schechter, A.N.3    Hogg, N.4
  • 42
    • 0033957066 scopus 로고    scopus 로고
    • Oxidation and erythrocyte senescence
    • DOI 10.1097/00062752-200003000-00007
    • Kiefer CR and Snyder LM. Oxidation and erythrocyte senescence. Curr Opin Hematol 7: 113-116, 2000. (Pubitemid 30106543)
    • (2000) Current Opinion in Hematology , vol.7 , Issue.2 , pp. 113-116
    • Kiefer, C.R.1    Snyder, L.M.2
  • 43
  • 45
    • 3142674792 scopus 로고    scopus 로고
    • 12, and iron
    • DOI 10.1146/annurev.nutr.24.012003.132306
    • Koury MJ and Ponka P. New insights into erythropoiesis: the roles of folate, vitamin B12, and iron. Annu Rev Nutr 24: 105-131, 2004. (Pubitemid 38938788)
    • (2004) Annual Review of Nutrition , vol.24 , pp. 105-131
    • Koury, M.J.1    Ponka, P.2
  • 48
    • 0019732571 scopus 로고
    • 2+ transport in human erythrocytes
    • Larsen FL, Katz S, and Roufogalis BD. Calmodulin regulation of Ca2 + transport in human erythrocytes. Biochem J 200: 185-191, 1981. (Pubitemid 12218242)
    • (1981) Biochemical Journal , vol.200 , Issue.2 , pp. 185-191
    • Larsen, F.L.1    Katz, S.2    Roufogalis, B.D.3
  • 49
    • 77950400027 scopus 로고    scopus 로고
    • Membrane remodeling during reticulocyte maturation
    • Liu J, Guo X, Mohandas N, Chasis JA, and An X. Membrane remodeling during reticulocyte maturation. Blood 115: 2021-2027, 2010.
    • (2010) Blood , vol.115 , pp. 2021-2027
    • Liu, J.1    Guo, X.2    Mohandas, N.3    Chasis, J.A.4    An, X.5
  • 50
    • 46449103811 scopus 로고    scopus 로고
    • Peroxiredoxin 2 and peroxide metabolism in the erythrocyte
    • Low FM, Hampton MB, and Winterbourn CC. Peroxiredoxin 2 and peroxide metabolism in the erythrocyte. Antioxid Redox Signal 10: 1621-1630, 2008.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1621-1630
    • Low, F.M.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 51
    • 0021969804 scopus 로고
    • The role of hemoglobin denaturation and band 3 clustering in red blood cell aging
    • Low PS, Waugh SM, Zinke K, and Drenckhahn D. The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science 227: 531-533, 1985. (Pubitemid 15153179)
    • (1985) Science , vol.227 , Issue.4686 , pp. 531-533
    • Low, P.S.1    Waugh, S.M.2    Zinke, K.3    Drenckhahn, D.4
  • 54
    • 0037181167 scopus 로고    scopus 로고
    • Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes
    • DOI 10.1016/S0014-5793(02)02294-9, PII S0014579302022949
    • Mandal D, Moitra PK, Saha S, and Basu J. Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes. FEBS Lett 513: 184-188, 2002. (Pubitemid 34251261)
    • (2002) FEBS Letters , vol.513 , Issue.2-3 , pp. 184-188
    • Mandal, D.1    Moitra, P.K.2    Saha, S.3    Basu, J.4
  • 56
    • 0029914963 scopus 로고    scopus 로고
    • Age-related change of phosphatidylcholine hydroperoxide and phosphatidylethanolamine hydroperoxide levels in normal human red blood cells
    • DOI 10.1016/0047-6374(95)01687-2
    • Miyazawa T, Suzuki T, Fujimoto K, and Kinoshita M. Age-related change of phosphatidylcholine hydroperoxide and phosphatidylethanolamine hydroperoxide levels in normal human red blood cells. Mech Ageing Dev 86: 145-150, 1996. (Pubitemid 26134551)
    • (1996) Mechanisms of Ageing and Development , vol.86 , Issue.3 , pp. 145-150
    • Miyazawa, T.1    Suzuki, T.2    Fujimoto, K.3    Kinoshita, M.4
  • 57
    • 58149158216 scopus 로고    scopus 로고
    • Red cell membrane: Past, present, and future
    • Mohandas N and Gallagher PG. Red cell membrane: past, present, and future. Blood 112: 3939-3948, 2008.
    • (2008) Blood , vol.112 , pp. 3939-3948
    • Mohandas, N.1    Gallagher, P.G.2
  • 58
    • 3242735024 scopus 로고    scopus 로고
    • Hydrogen-peroxide-induced heme degradation in red blood cells: The protective roles of catalase and glutathione peroxidase
    • DOI 10.1016/S0304-4165(02)00537-8
    • Nagababu E, Chrest FJ, and Rifkind JM. Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase. Biochim Biophys Acta 1620: 211-217, 2003. (Pubitemid 36197913)
    • (2003) Biochimica et Biophysica Acta - General Subjects , vol.1620 , Issue.1-3 , pp. 211-217
    • Nagababu, E.1    Chrest, F.J.2    Rifkind, J.M.3
  • 59
    • 44649126828 scopus 로고    scopus 로고
    • Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease
    • Nagababu E, Fabry ME, Nagel RL, and Rifkind JM. Heme degradation and oxidative stress in murine models for hemoglobinopathies: thalassemia, sickle cell disease and hemoglobin C disease. Blood Cells Mol Dis 41: 60-66, 2008.
    • (2008) Blood Cells Mol Dis , vol.41 , pp. 60-66
    • Nagababu, E.1    Fabry, M.E.2    Nagel, R.L.3    Rifkind, J.M.4
  • 61
    • 73549114427 scopus 로고    scopus 로고
    • Role of the membrane in the formation of heme degradation products in red blood cells
    • Nagababu E, Mohanty JG, Bhamidipaty S, Ostera GR, and Rifkind JM. Role of the membrane in the formation of heme degradation products in red blood cells. Life Sci 86: 133-138, 2010.
    • (2010) Life Sci , vol.86 , pp. 133-138
    • Nagababu, E.1    Mohanty, J.G.2    Bhamidipaty, S.3    Ostera, G.R.4    Rifkind, J.M.5
  • 62
    • 0344443777 scopus 로고    scopus 로고
    • Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction
    • DOI 10.1074/jbc.M307572200
    • Nagababu E, Ramasamy S, Abernethy DR, and Rifkind JM. Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction. J Biol Chem 278: 46349-46356, 2003. (Pubitemid 37452205)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46349-46356
    • Nagababu, E.1    Ramasamy, S.2    Abernethy, D.R.3    Rifkind, J.M.4
  • 63
    • 0037062603 scopus 로고    scopus 로고
    • Site-specific cross-linking of human and bovine hemoglobins differentially alters oxygen binding and redox side reactions producing rhombic heme and heme degradation
    • DOI 10.1021/bi0121048
    • Nagababu E, Ramasamy S, Rifkind JM, Jia Y, and Alayash AI. Site-specific cross-linking of human and bovine hemoglobins differentially alters oxygen binding and redox side reactions producing rhombic heme and heme degradation. Biochemistry 41: 7407-7415, 2002. (Pubitemid 34602459)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7407-7415
    • Nagababu, E.1    Ramasamy, S.2    Rifkind, J.M.3    Jia, Y.4    Alayash, A.I.5
  • 64
    • 0032577878 scopus 로고    scopus 로고
    • Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide
    • DOI 10.1006/bbrc.1998.8846
    • Nagababu E and Rifkind JM. Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide. Biochem Biophys Res Commun 247: 592-596, 1998. (Pubitemid 28418436)
    • (1998) Biochemical and Biophysical Research Communications , vol.247 , Issue.3 , pp. 592-596
    • Nagababu, E.1    Rifkind, J.M.2
  • 66
    • 0034633998 scopus 로고    scopus 로고
    • Reaction of hydrogen peroxide with ferrylhemoglobin: Superoxide production and heme degradation
    • Nagababu E and Rifkind JM. Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation. Biochemistry 39: 12503-12511, 2000.
    • (2000) Biochemistry , vol.39 , pp. 12503-12511
    • Nagababu, E.1    Rifkind, J.M.2
  • 67
    • 7244240720 scopus 로고    scopus 로고
    • Heme degradation by reactive oxygen species
    • DOI 10.1089/ars.2004.6.967
    • Nagababu E and Rifkind JM. Heme degradation by reactive oxygen species. Antioxid Redox Signal 6: 967-978, 2004. (Pubitemid 39434933)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.6 , pp. 967-978
    • Nagababu, E.1    Rifkind, J.M.2
  • 68
    • 33947274050 scopus 로고    scopus 로고
    • Measurement of plasma nitrite by chemiluminescence without interference of S-, N-nitroso and nitrated species
    • DOI 10.1016/j.freeradbiomed.2006.12.029, PII S0891584907000056
    • Nagababu E and Rifkind JM. Measurement of plasma nitrite by chemiluminescence without interference of S-, N-nitroso and nitrated species. Free Radic Biol Med 42: 1146-1154, 2007. (Pubitemid 46428509)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.8 , pp. 1146-1154
    • Nagababu, E.1    Rifkind, J.M.2
  • 69
    • 0032169398 scopus 로고    scopus 로고
    • The effects of xenobiotics on erythrocytes
    • DOI 10.1016/S0306-3623(97)00457-6, PII S0306362397004576
    • Nohl H and Stolze K. The effects of xenobiotics on erythrocytes. Gen Pharmacol 31: 343-347, 1998. (Pubitemid 28398856)
    • (1998) General Pharmacology , vol.31 , Issue.3 , pp. 343-347
    • Nohl, H.1    Stolze, K.2
  • 70
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • DOI 10.1152/physrev.00029.2006
    • Pacher P, Beckman JS, and Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol Rev 87: 315-424, 2007. (Pubitemid 46217686)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 72
    • 0028796836 scopus 로고
    • Oxidation state of glutathione and membrane proteins in human red cells of different age
    • Piccinini G, Minetti G, Balduini C, and Brovelli A. Oxidation state of glutathione and membrane proteins in human red cells of different age. Mech Ageing Dev 78: 15-26, 1995.
    • (1995) Mech Ageing Dev , vol.78 , pp. 15-26
    • Piccinini, G.1    Minetti, G.2    Balduini, C.3    Brovelli, A.4
  • 73
    • 0035909807 scopus 로고    scopus 로고
    • 2 inhibits heme-catalyzed scavenging and isomerization
    • DOI 10.1021/bi010998q
    • Pietraforte D, Salzano AM, Scorza G, Marino G, and Minetti M. Mechanism of peroxynitrite interaction with ferric hemoglobin and identification of nitrated tyrosine residues. CO(2) inhibits heme-catalyzed scavenging and isomerization. Biochemistry 40: 15300-15309, 2001. (Pubitemid 33151944)
    • (2001) Biochemistry , vol.40 , Issue.50 , pp. 15300-15309
    • Pietraforte, D.1    Maria Salzano, A.2    Scorza, G.3    Marino, G.4    Minetti, M.5
  • 74
    • 0027463316 scopus 로고
    • Mechanism of red blood cell aging: Relationship of cell density and cell age
    • DOI 10.1002/ajh.2830420110
    • Piomelli S and Seaman C. Mechanism of red blood cell aging: relationship of cell density and cell age. Am J Hematol 42: 46-52, 1993. (Pubitemid 23008311)
    • (1993) American Journal of Hematology , vol.42 , Issue.1 , pp. 46-52
    • Piomelli, S.1    Seaman, C.2
  • 75
    • 25144453937 scopus 로고    scopus 로고
    • NADPH oxidase and endothelial cell function
    • DOI 10.1042/CS20050067
    • Ray R and Shah AM. NADPH oxidase and endothelial cell function. Clin Sci (Lond) 109: 217-226, 2005. (Pubitemid 41337126)
    • (2005) Clinical Science , vol.109 , Issue.3 , pp. 217-226
    • Ray, R.1    Shah, A.M.2
  • 76
    • 0026020956 scopus 로고
    • Calcium-stressed erythrocyte membrane structure and function for assessing glipizide effects on transglutaminase activation
    • Redding GS, Record DM, and Raess BU. Calcium-stressed erythrocyte membrane structure and function for assessing glipizide effects on transglutaminase activation. Proc Soc Exp Biol Med 196: 76-82, 1991.
    • (1991) Proc Soc Exp Biol Med , vol.196 , pp. 76-82
    • Redding, G.S.1    Record, D.M.2    Raess, B.U.3
  • 77
    • 0032939337 scopus 로고    scopus 로고
    • Evaluation of biochemical changes during in vivo erythrocyte senescence in the dog
    • Rettig MP, Low PS, Gimm JA, Mohandas N, Wang J, and Christian JA. Evaluation of biochemical changes during in vivo erythrocyte senescence in the dog. Blood 93: 376-384, 1999. (Pubitemid 29019426)
    • (1999) Blood , vol.93 , Issue.1 , pp. 376-384
    • Rettig, M.P.1    Low Philip, S.P.S.2    Gimm, J.A.3    Mohandas, N.4    Wang, J.5    Christian, J.A.6
  • 78
    • 84876901432 scopus 로고    scopus 로고
    • Heme iron in hemoglobin and myoglobin
    • edited by Fuchs H, Mohanty JG, Nagababu E, Ramasamy S, and Ravi L. Trivandrum, Kerala, India: Research Signpost
    • Rifkind JM. Heme iron in hemoglobin and myoglobin. In: Iron Metabolism and Diseases, edited by Fuchs H, Mohanty JG, Nagababu E, Ramasamy S, and Ravi L. Trivandrum, Kerala, India: Research Signpost, 2008, pp. 365-392.
    • (2008) Iron Metabolism and Diseases , pp. 365-392
    • Rifkind, J.M.1
  • 79
    • 0028625636 scopus 로고
    • Alterations in erythrocyte deformability under hypoxia: Implications for impaired oxygen transport
    • Rifkind JM and Abugo OO. Alterations in erythrocyte deformability under hypoxia: implications for impaired oxygen transport. Adv Exp Med Biol 361: 345-351, 1994.
    • (1994) Adv Exp Med Biol , vol.361 , pp. 345-351
    • Rifkind, J.M.1    Abugo, O.O.2
  • 80
    • 33746788491 scopus 로고    scopus 로고
    • Nitric oxide redox reactions and red cell biology
    • DOI 10.1089/ars.2006.8.1193
    • Rifkind JM, Nagababu E, and Ramasamy S. Nitric oxide redox reactions and red cell biology. Antioxid Redox Signal 8: 1193-1203, 2006. (Pubitemid 44182418)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.7-8 , pp. 1193-1203
    • Rifkind, J.M.1    Nagababu, E.2    Ramasamy, S.3
  • 81
    • 79951680255 scopus 로고    scopus 로고
    • The quaternary hemoglobin conformation regulates the formation of the nitrite-induced bioactive intermediate and the dissociation of nitric oxide from this intermediate
    • Rifkind JM, Nagababu E, and Ramasamy S. The quaternary hemoglobin conformation regulates the formation of the nitrite-induced bioactive intermediate and the dissociation of nitric oxide from this intermediate. Nitric Oxide 24: 102-109, 2011.
    • (2011) Nitric Oxide , vol.24 , pp. 102-109
    • Rifkind, J.M.1    Nagababu, E.2    Ramasamy, S.3
  • 83
    • 84856247386 scopus 로고    scopus 로고
    • Regulation of oxygen delivery by the reaction of nitrite with RBCs under hypoxic conditions
    • Rifkind JM, Salgado MT, and Cao Z. Regulation of oxygen delivery by the reaction of nitrite with RBCs under hypoxic conditions. Adv Exp Med Biol 737: 183-189, 2012.
    • (2012) Adv Exp Med Biol , vol.737 , pp. 183-189
    • Rifkind, J.M.1    Salgado, M.T.2    Cao, Z.3
  • 84
    • 84907037913 scopus 로고
    • The hypoxic stress on erythrocytes associated with superoxide formation
    • Rifkind JM, Zhang L, Levy A, and Manoharan PT. The hypoxic stress on erythrocytes associated with superoxide formation. Free Radic Res Commun 12-13 Pt 2: 645-652, 1991.
    • (1991) Free Radic Res Commun , vol.12-13 , Issue.PART 2 , pp. 645-652
    • Rifkind, J.M.1    Zhang, L.2    Levy, A.3    Manoharan, P.T.4
  • 85
    • 70349323591 scopus 로고    scopus 로고
    • Hypoxia limits antioxidant capacity in red blood cells by altering glycolytic pathway dominance
    • Rogers SC, Said A, Corcuera D, McLaughlin D, Kell P, and Doctor A. Hypoxia limits antioxidant capacity in red blood cells by altering glycolytic pathway dominance. FASEB J 23: 3159-3170, 2009.
    • (2009) FASEB J , vol.23 , pp. 3159-3170
    • Rogers, S.C.1    Said, A.2    Corcuera, D.3    McLaughlin, D.4    Kell, P.5    Doctor, A.6
  • 86
    • 33749504772 scopus 로고    scopus 로고
    • Red blood cells in the metabolism of nitric oxide-derived peroxynitrite
    • DOI 10.1080/15216540600936549, PII R4835737K745NX1W
    • Romero N, Denicola A, and Radi R. Red blood cells in the metabolism of nitric oxide-derived peroxynitrite. IUBMB Life 58: 572-580, 2006. (Pubitemid 44527221)
    • (2006) IUBMB Life , vol.58 , Issue.10 , pp. 572-580
    • Romero, N.1    Denicola, A.2    Radi, R.3
  • 87
    • 27744543545 scopus 로고    scopus 로고
    • Hemoglobin and red blood cells as tools for studying peroxynitrite biochemistry
    • DOI 10.1016/S0076-6879(05)96021-7, PII S0076687905960217, Nitric Oxide
    • Romero N and Radi R. Hemoglobin and red blood cells as tools for studying peroxynitrite biochemistry. Methods Enzymol 396: 229-245, 2005. (Pubitemid 41603551)
    • (2005) Methods in Enzymology , vol.396 , pp. 229-245
    • Romero, N.1    Radi, R.2
  • 88
    • 67649786604 scopus 로고    scopus 로고
    • Quantification of intermediates formed during the reduction of nitrite by deoxyhemoglobin
    • Salgado MT, Nagababu E, and Rifkind JM. Quantification of intermediates formed during the reduction of nitrite by deoxyhemoglobin. J Biol Chem 284: 12710-12718, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 12710-12718
    • Salgado, M.T.1    Nagababu, E.2    Rifkind, J.M.3
  • 89
    • 80051759193 scopus 로고    scopus 로고
    • A new paramagnetic intermediate formed during the reaction of nitrite with deoxyhemoglobin
    • Salgado MT, Ramasamy S, Tsuneshige A, Manoharan PT, and Rifkind JM. A new paramagnetic intermediate formed during the reaction of nitrite with deoxyhemoglobin. J Am Chem Soc 133: 13010-13022, 2011.
    • (2011) J Am Chem Soc , vol.133 , pp. 13010-13022
    • Salgado, M.T.1    Ramasamy, S.2    Tsuneshige, A.3    Manoharan, P.T.4    Rifkind, J.M.5
  • 91
    • 0022784193 scopus 로고
    • Disintegration of red cell membrane cytoskeleton by hemin
    • Shaklai N, Avissar N, Rabizadeh E, and Shaklai M. Disintegration of red cell membrane cytoskeleton by hemin. Biochem Int 13: 467-477, 1986.
    • (1986) Biochem Int , vol.13 , pp. 467-477
    • Shaklai, N.1    Avissar, N.2    Rabizadeh, E.3    Shaklai, M.4
  • 93
    • 0023472083 scopus 로고
    • Glutathione as a scavenger of free hemin. A mechanism of preventing red cell membrane damage
    • DOI 10.1016/0006-2952(87)90441-2
    • Shviro Y and Shaklai N. Glutathione as a scavenger of free hemin. A mechanism of preventing red cell membrane damage. Biochem Pharmacol 36: 3801-3807, 1987. (Pubitemid 18010938)
    • (1987) Biochemical Pharmacology , vol.36 , Issue.22 , pp. 3801-3807
    • Shviro, Y.1    Shaklai, N.2
  • 95
    • 0023275935 scopus 로고
    • Adenine and pyridine nucleotides during rabbit reticulocyte maturation and cell aging
    • DOI 10.1016/0047-6374(87)90084-4
    • Stocchi V, Kolb N, Cucchiarini L, Segni M, Magnani M, and Fornaini G. Adenine, and pyridine nucleotides during rabbit reticulocyte maturation and cell aging. Mech Ageing Dev 39: 29-44, 1987. (Pubitemid 17091158)
    • (1987) Mechanisms of Ageing and Development , vol.39 , Issue.1 , pp. 29-44
    • Stocchi, V.1    Kolb, N.2    Cucchiarini, L.3
  • 96
    • 36148998364 scopus 로고    scopus 로고
    • Participation of caspase-3-like protease in oxidation-induced impairment of erythrocyte membrane properties
    • Suzuki Y, Ohkubo N, Aoto M, Maeda N, Cicha I, Miki T, and Mitsuda N. Participation of caspase-3-like protease in oxidation-induced impairment of erythrocyte membrane properties. Biorheology 44: 179-190, 2007. (Pubitemid 350114366)
    • (2007) Biorheology , vol.44 , Issue.3 , pp. 179-190
    • Suzuki, Y.1    Ohkubo, N.2    Aoto, M.3    Maeda, N.4    Cicha, I.5    Miki, T.6    Mitsuda, N.7
  • 97
    • 77953768762 scopus 로고    scopus 로고
    • AMPKalpha1 deletion shortens erythrocyte life span in mice: Role of oxidative stress
    • Wang S, Dale GL, Song P, Viollet B, and Zou MH. AMPKalpha1 deletion shortens erythrocyte life span in mice: role of oxidative stress. J Biol Chem 285: 19976-19985, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 19976-19985
    • Wang, S.1    Dale, G.L.2    Song, P.3    Viollet, B.4    Zou, M.H.5
  • 98
    • 0026503909 scopus 로고
    • Rheologic properties of senescent erythrocytes: Loss of surface area and volume with red blood cell age
    • Waugh RE, Narla M, Jackson CW, Mueller TJ, Suzuki T, and Dale GL. Rheologic properties of senescent erythrocytes: loss of surface area and volume with red blood cell age. Blood 79: 1351-1358, 1992.
    • (1992) Blood , vol.79 , pp. 1351-1358
    • Waugh, R.E.1    Narla, M.2    Jackson, C.W.3    Mueller, T.J.4    Suzuki, T.5    Dale, G.L.6
  • 99
    • 84864470278 scopus 로고    scopus 로고
    • Role of calcium in phosphatidylserine externalisation in red blood cells from sickle cell patients
    • Weiss E, Rees DC, and Gibson JS. Role of calcium in phosphatidylserine externalisation in red blood cells from sickle cell patients. Anemia 2011: 379894, 2011.
    • (2011) Anemia , vol.2011 , pp. 379894
    • Weiss, E.1    Rees, D.C.2    Gibson, J.S.3
  • 102
    • 0024496720 scopus 로고
    • Interaction of hemin with erythrocyte membranes: Alterations in the physical state of the major sialoglycoprotein
    • DOI 10.1016/0005-2736(89)90531-2
    • Wyse JW and Butterfield DA. Interaction of hemin with erythrocyte membranes: alterations in the physical state of the major sialoglycoprotein. Biochim Biophys Acta 979: 121-126, 1989. (Pubitemid 19050052)
    • (1989) Biochimica et Biophysica Acta - Biomembranes , vol.979 , Issue.1 , pp. 121-126
    • Wyse, J.W.1    Butterfield, D.A.2
  • 103
    • 80053369909 scopus 로고    scopus 로고
    • A novel approach for in vivo measurement of mouse red cell redox status
    • Xu X, von LK, Soldau K, Noack D, Vu A, and Friedman JS. A novel approach for in vivo measurement of mouse red cell redox status. Blood 118: 3694-3697, 2011.
    • (2011) Blood , vol.118 , pp. 3694-3697
    • Xu, X.1    Von Lk Soldau, K.2    Noack, D.3    Vu, A.4    Friedman, J.S.5
  • 104
    • 0025254048 scopus 로고
    • In vivo aging of red cell enzymes: Study of biotinylated red blood cells in rabbits
    • Zimran A, Forman L, Suzuki T, Dale GL, and Beutler E. In vivo aging of red cell enzymes: study of biotinylated red blood cells in rabbits. Am J Hematol 33: 249-254, 1990. (Pubitemid 20116292)
    • (1990) American Journal of Hematology , vol.33 , Issue.4 , pp. 249-254
    • Zimran, A.1    Forman, L.2    Suzuki, T.3    Dale, G.L.4    Beutler, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.